Mimicking Class I b Mn2‐Ribonucleotide Reductase: A MnII2 Complex and Its Reaction with Superoxide

Abstract

AbstractA fascinating discovery in the chemistry of ribonucleotide reductases (RNRs) has been the identification of a dimanganese (Mn2) active site in class I b RNRs that requires superoxide anion (O2.−), rather than dioxygen (O2), to access a high‐valent Mn2 oxidant. Complex 1 ([Mn2(O2CCH3)(N‐Et‐HPTB)](ClO4)2, N‐Et‐HPTB=N,N,N′,N′‐tetrakis(2‐(1‐ethylbenzimidazolyl))‐2‐hydroxy‐1,3‐diaminopropane) was synthesised in high yield (90 %). 1 was reacted with O2.− at −40 °C resulting in the formation of a metastable species (2). 2 displayed electronic absorption features (λmax=460, 610 nm) typical of a Mn‐peroxide species and a 29‐line EPR signal typical of a MnIIMnIII entity. Mn K‐edge X‐ray absorption near‐edge spectroscopy (XANES) suggested a formal oxidation state change of MnII2 in 1 to MnIIMnIII for 2. Electrospray ionisation mass spectrometry (ESI‐MS) suggested 2 to be a MnIIMnIII‐peroxide complex. 2 was capable of oxidizing ferrocene and weak O−H bonds upon activation with proton donors. Our findings provide support for the postulated mechanism of O2.− activation at class I b Mn2 RNRs.